Switching the proton-coupled electron transfer mechanism for non-canonical tyrosine residues in a de novo protein

Author:

Nilsen-Moe Astrid1,Reinhardt Clorice R.2ORCID,Huang Ping1ORCID,Agarwala Hemlata3,Lopes Rosana4ORCID,Lasagna Mauricio4ORCID,Glover Starla1,Hammes-Schiffer Sharon5ORCID,Tommos Cecilia4ORCID,Hammarström Leif1ORCID

Affiliation:

1. Department of Chemistry, Ångström Laboratory, Uppsala University, Box 523, 75120 Uppsala, Sweden

2. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA

3. Technical University Munich, Campus Straubing for Biotechnology and Sustainability, Uferstraße 53, 94315 Straubing, Germany

4. Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA

5. Department of Chemistry, Yale University, New Haven, CT 06520, USA

Abstract

Proton-coupled electron transfer reactions of tyrosine are instrumental to many redox reactions in nature. By balancing the driving forces for electron and proton transfer, the mechanism can be changed from step-wise to concerted transfer (CEPT).

Funder

National Science Foundation Graduate Research Fellowship Program

National Institutes of Health

Vetenskapsrådet

Publisher

Royal Society of Chemistry (RSC)

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